Srinivas Bharath, MM and Khadake, JR and Rao, MRS (1998) Expression of rat histone H1d in Escherichia coli and its purification. In: Protein Expression and Purification, 12 (01). pp. 38-44.
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Abstract
Histone H1 is involved in the folding of linear polynucleosomal filament into a 30-nm fiber. In an effort to understand the role of different domains of histone H1 in chromatin folding, we have now expressed rat histone H1d in Escherichia coli using pTrc99A expression vector by providing a 6-His tag at the C-terminus to facilitate its purification, The expressed protein histone H1d was purified from the soluble extract of E. coli by employing Ni2+ NTA-agarose and heparin-agarose chromatography. The recombinant histone H1d was shown to be authentic by its N-terminal amino acid analysis, its secondary structural characteristics, and its ability to (a) condense DNA and (b) bind specifically to synthetic four-way junction DNA
Item Type: | Journal Article |
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Publication: | Protein Expression and Purification |
Publisher: | Elsevier Science |
Additional Information: | Copyright of this article belongs to Elsevier Sciences. |
Department/Centre: | Division of Biological Sciences > Biochemistry |
Date Deposited: | 19 Jul 2009 06:39 |
Last Modified: | 19 Sep 2010 05:24 |
URI: | http://eprints.iisc.ac.in/id/eprint/18642 |
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